A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation.

ABSTRACT: BRICHOS is a domain found in several proteins consisting of approximately 100 amino acids with sequence and structural similarities. Mutations in BRICHOS domain have been associated with both degenerative and proliferative diseases in several nonpulmonary organs, although the pathogenic mechanisms are largely undefined. Recently, several mutations in surfactant protein C (SP-C) mapping to the BRICHOS domain located within the proprotein (proSP-C) have been linked to interstitial lung diseases. In vitro expression of one of these BRICHOS mutants, the exon 4 deletion (hSP-CDeltaexon4), promotes a dominant-negative perinuclear aggregation of the protein. The present study characterizes the trafficking behavior and pathogenic consequences resulting from hSP-CDeltaexon4 expression. Time-lapse a

SUBMITTER: Mulugeta S 

PROVIDER: S-EPMC2715321 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature